Year: 2021
Type: review
Abstract: Disrupted protein folding or decreased protein stability can lead to the accumulation of (partially) un- or misfolded proteins, which ultimately cause the formation of protein aggregates. Much of the interest in protein aggregation is associated with its involvement in a wide range of human diseases and the challenges it poses for large-scale biopharmaceutical manufacturing and formulation of therapeutic proteins and peptides. On the other hand, protein aggregates can also be functional, as observed in nature, which triggered its use in the development of biomaterials or therapeutics as well as for the improvement of food characteristics. Thus, unmasking the various steps involved in protein aggregation is critical to obtain a better understanding of the underlying mechanism of amyloid formation. This knowledge will allow a more tailored development of diagnostic methods and treatments for amyloid-associated diseases, as well as applications in the fields of new (bio)materials, food technology and therapeutics. However, the complex and dynamic nature of the aggregation process makes the study of protein aggregation challenging. To provide guidance on how to analyse protein aggregation, in this review we summarize the most commonly investigated aspects of protein aggregation with some popular corresponding methods.
Source: FEBS Journal
DOI: 10.1111/febs.16312
Institutions: VIB-KU Leuven Center for Brain & Disease Research, KU Leuven
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Awards: Atomic Force Microscopy Enhanced Spectroscopy to Study Strains and Seeding of Amyloids In Situ, Knowledge platform: tailoring food protein functionality by rational design of fibrillar structures (PROFIBFUN), High throughput analysis of biomolecular interactions, G8406824037, A 200 kV Transmission Electron Microscope for high-resolution determination of 3D-ultrastructure of native proteins, cells and tissue.
OpenAlex ID: W3216255697